H3F3B Mouse Monoclonal Antibody
- Known as:
- H3F3B Mouse Monoclonal Antibody
- Catalog number:
- BIN-003021-M01
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- H3F3B Mouse Monoclonal Antibody
Related genes to: H3F3B Mouse Monoclonal Antibody
- Gene:
- H3F3B NIH gene
- Name:
- H3 histone family member 3B
- Previous symbol:
- -
- Synonyms:
- H3.3B
- Chromosome:
- 17q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-10-02
- Date modifiied:
- 2016-08-12
Related products to: H3F3B Mouse Monoclonal Antibody
Related articles to: H3F3B Mouse Monoclonal Antibody
- To evaluate the association between genetic mutations and clinical outcomes, including response and time to progression, in patients with breast cancer liver metastasis treated with Y-90 radioembolization. - Source: PubMed
Publication date: 2026/04/21
Daana BajnauthAmy DeipolyiFrank AnnieYolanda Bryce - Giant cell tumor of bone (GCTB) is a rare, locally aggressive, intermediate-grade neoplasm. While typically benign, GCTB can exhibit atypical behavior, including indolent pulmonary metastases and malignant transformation. This study characterizes malignant and metastatic GCTB, distinguishing primary malignant GCTB (PM-GCTB), secondary malignant GCTB (SM-GCTB), and secondary osteosarcoma, and evaluates their outcomes. - Source: PubMed
Publication date: 2025/11/24
Verspoor Floortje G MKrebbekx Gitte G JDuivenvoorden Mylene J CSumathi VaiyapuriEvans Scott - Neutrophil extracellular traps (NETs) are chomatin-based structures that contribute to the defense mechanisms of a host; however, NETs can also drive inflammation when dysregulated. Particulate matter (PM), a major air pollutant, has been shown to induce the formation of NETs, yet the impact of PM on peroxisomal homeostasis in neutrophils remains poorly understood. Thus, this study aimed to examine the effects of PM exposure on NETosis and peroxisomal dynamics in bone marrow-derived neutrophils (BMDNs) and differentiated HL-60 (dHL-60) cells. RNA sequencing was performed on PM-treated BMDNs, identifying 2436 differentially expressed genes (DEGs). These included the upregulation of NETosis-related genes (Padi4, Mpo, H3f3b) and genes involved in peroxisomal quality control and degradation, such as Pex5, Ubb, Rps27a, Nbr1, Map1lc3b, and Sqstm1. Functionally, PM exposure (50-100 μg/mL) increased reactive oxygen species (ROS) levels and induced PAD4 and citrullinated histone H3 (citH3) expression, indicating that NETosis is dependent on ROS. In parallel, peroxisomal markers, including ACOX1, PEX5, PMP70, and catalase, were dynamically regulated. Despite transient upregulation of peroxisomal markers, pexophagy was activated, as shown by increased levels of p62, beclin-1, NBR1, and LC3B, and colocalization of LC3B with peroxisomal protein PEX13. Both ROS inhibition by DPI or NAC and NET inhibition by Cl-amidine significantly attenuated pexophagy activation, indicating that PM-induced peroxisomal degradation is driven by ROS-dependent NET formation. These results reveal a ROS-NET-peroxisome axis in PM-induced neutrophil activation, offering novel insights into immune dysregulation under environmental stress and identifying potential targets for PM-induced inflammation. - Source: PubMed
Publication date: 2025/11/14
Shin YejiKim KahyunHan JisooKim ByounghwaLim Hyun JoungUm Jae-YoungLee InhyungKwak Hyun Jeong - Histones are the fundamental building blocks of chromatin and serve as pivotal regulators of gene expression. Differential expression and mutations of H3.1 and H3.3 genes have been implicated in the pathogenesis of various cancer types. Mutations in H3.3, especially lysine to methionine substitutions (K27M/K36M), are particularly prevalent. Moreover, genetic alterations such as G34R/W/V/L, as well as variations in and genes, have also been identified. Despite high similarity in amino acid sequences, H3.1 and H3.3 have discrete functions in cancer. In this review, we delve into the recent advances in elucidating the implications of canonical histone H3.1 and its variant H3.3 on chromatin structure and function. Additionally, we explore how potential enhancing factors such as PTEN, MLL5, GPR87 and histone chaperones influence H3.1/H3.3 function. - Source: PubMed
Publication date: 2025/09/24
Wu PengWang LiWen TingChen Qiao Yi - H3K27-altered diffuse midline glioma (DMG) is a fatal disease, including four subtypes H3.3-mutant, H3.1/H3.2-mutant, H3-wildtype with EZHIP overexpression, and EGFR-mutant. H3F3B, another gene encoding histone H3.3 in addition to H3F3A, was ever reported to be mutated in DMGs. However, the clinical and molecular characteristics of H3F3B-mutant DMGs is yet understood. The clinical and radiological information of 9 patients with H3F3B-mutant DMG were retrospectively collected. Tumor specimens underwent DNA methylation profiling and next-generation sequencing. All tumors harbored somatic H3F3B p.K27I mutation. Average patient age was 46 ± 6.86 years, 6 tumors located in spinal cord, 5 tumors involved brainstem and 2 arose in the thalamus. Immunohistochemistry showed these tumors exhibited completely or mosaic-like loss of H3K27me3 expression. Unsupervised t-distributed stochastic neighbor embedding (t-SNE) analysis of DNA methylation profiles showed that H3F3B-mutant DMGs formed a unique methylation cluster separate from other gliomas with H3K27me3 loss and DMGs with canonical histone H3 mutation. PPM1D and NF1 were frequently mutated in H3F3B-mutant DMGs. Survival analysis showed that H3F3B-mutant DMGs had poor prognosis comparable to H3K27M-mutant DMGs. Taken together, H3F3B mutation also cause a loss of H3K27 trimethylation in DMGs and result in poor prognosis. The distinct characteristics of DNA methylation and mutational spectrum between H3F3B-mutant DMGs and canonical H3K27M-mutant DMGs might suggest divergent underlying mechanism of gliomagenesis. - Source: PubMed
Publication date: 2025/08/23
Cheng LeiZhou MinLuo TaoDong RongfangChen NiCai XinyongWang XingwenWu HaoChen ZanWang ZuoweiQi XuelingLu DehongTeng LianghongJian FengzengWang Leiming